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Cited by 731Plant Stress Responses and TolerancePlant Molecular Biology ResearchSeed Germination and Physiology

A gate–latch–lock mechanism for hormone signalling by abscisic acid receptors

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Melcher, Karsten, Ng, Ley-Moy, Zhou, X. Edward, Soon, Fen-Fen, Xu, Yong, Suino-Powell, Kelly M., Park, Sang-Youl, Weiner, Joshua J. +13 more·2009·Nature
DOI 10.1038/nature08613PMC PMC2810868
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Abstract

Abscisic acid (ABA) is a ubiquitous hormone that regulates plant growth, development and responses to environmental stresses. Its action is mediated by the PYR/PYL/RCAR family of START proteins, but it remains unclear how these receptors bind ABA and, in turn, how hormone binding leads to inhibition of the downstream type 2C protein phosphatase (PP2C) effectors. Here we report crystal structures of apo and ABA-bound receptors as well as a ternary PYL2-ABA-PP2C complex. The apo receptors contain an open ligand-binding pocket flanked by a gate that closes in response to ABA by way of conformational changes in two highly conserved beta-loops that serve as a gate and latch. Moreover, ABA-induced closure of the gate creates a surface that enables the receptor to dock into and competitively inhibit the PP2C active site. A conserved tryptophan in the PP2C inserts directly between the gate and latch, which functions to further lock the receptor in a closed conformation. Together, our results identify a conserved gate-latch-lock mechanism underlying ABA signalling.

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Authors
Melcher, K., Ng, L.-M., Zhou, X. E., Soon, F.-F., Xu, Y., Suino-Powell, K. M., Park, S.-Y., Weiner, J. J., Fujii, H., Chinnusamy, V., Kovach, A., Li, J., Wang, Y., Li, J., Peterson, F. C., Jensen, D. R., Yong, E.-L., Volkman, B. F., Cutler, S. R., Zhu, J.-K., & Xu, H. E.
Affiliations
  • Van Andel Institute (US)
  • University of California, Riverside (US)
  • Medical College of Wisconsin (US)
  • Chinese Academy of Sciences (CN)
  • National University of Singapore (SG)
Corresponding author
Xu, H. Eric
ORCID
Venue
Nature
Publisher
Springer Science and Business Media LLC
Published
2009-11-06
Volume
462
Issue
7273
Pages
602-608
ISSN
  • 0028-0836 (ISSN-L)
  • 1476-4687
DOI
10.1038/nature08613
PMC
PMC2810868
OpenAlex
W2155619616
Cited by
731
References
1
Citations by year
2026: 33 · 2025: 43 · 2024: 49 · 2023: 35 · 2022: 39 · 2021: 48 · 2020: 50 · 2019: 53 · 2018: 33 · 2017: 46 · 2016: 25 · 2015: 40 · 2014: 43 · 2013: 44 · 2012: 39
FWCI
60.31
Type
journal article
Language
en
Open access
Licence
www.springer.com/tdm (tdm)
Locations
  • Nature (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
  • RePEc: Research Papers in Economics (submittedVersion)
  • King Abdullah University of Science and Technology Repository (King Abdullah University of Science and Technology) (submittedVersion)
Funders
  • National Heart, Lung, and Blood Institute (R01HL089301)
  • National Institute of General Medical Sciences (R01GM087413)
  • National Institute of Diabetes and Digestive and Kidney Diseases (R01DK066202, R01DK071662)
Topics
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Stress Responses and Tolerance
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Seed Germination and Physiology
Keywords
abscisic acid signaling, PYR/PYL/RCAR receptors, protein phosphatase 2C, binding pocket, receptor conformational change, ABI1, ABI2, plant hormone receptors
MeSH terms
Abscisic Acid, Binding Sites, DNA Mutational Analysis, Models, Molecular, Protein Binding, Signal Transduction, Arabidopsis, Protein Structure, Tertiary, Arabidopsis Proteins, Plants, Genetically Modified

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